Identification and characterization of α-xylosidase involved in xyloglucan degradation in Aspergillus oryzae
Identification and characterization of α-xylosidase involved in xyloglucan degradation in Aspergillus oryzae
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DOI:
10.1007/s00253-019-10244-z
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发表时间:
2019-11-28
影响因子:
5
通讯作者:
Yaoi, Katsuro
中科院分区:
文献类型:
--
作者:
Matsuzawa, Tomohiko;Kameyama, Akihiko;Yaoi, Katsuro
Aspergillus oryzae produces hydrolases involved in xyloglucan degradation and induces the expression of genes encoding xyloglucan oligosaccharide hydrolases in the presence of xyloglucan oligosaccharides. A gene encoding alpha-xylosidase (termed AxyA), which is induced in the presence of xyloglucan oligosaccharides, is identified and expressed in Pichia pastoris. AxyA is a member of the glycoside hydrolase family 31 (GH31). AxyA hydrolyzes isoprimeverose (alpha-d-xylopyranosyl-(1 -> 6)-d-glucopyranose) into d-xylose and d-glucose and shows hydrolytic activity with other xyloglucan oligosaccharides such as XXXG (heptasaccharide, Glc(4)Xyl(3)) and XLLG (nonasaccharide, Glc(4)Xyl(3)Gal(2)). Isoprimeverose is a preferred AxyA substrate over other xyloglucan oligosaccharides. In the hydrolysis of XXXG, AxyA releases one molecule of d-xylose from one molecule of XXXG to yield GXXG (hexasaccharide, Glc(4)Xyl(2)). AxyA does not contain a signal peptide for secretion and remains within the cell. The intracellular localization of AxyA may help determine the order of hydrolases acting on xyloglucan oligosaccharides.